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Chlorine in PDB 1yml: Crystal Structure of the CDC25B Phosphatase Catalytic Domain with the Active Site Cysteine in the Sulfenic Form

Enzymatic activity of Crystal Structure of the CDC25B Phosphatase Catalytic Domain with the Active Site Cysteine in the Sulfenic Form

All present enzymatic activity of Crystal Structure of the CDC25B Phosphatase Catalytic Domain with the Active Site Cysteine in the Sulfenic Form:
3.1.3.48;

Protein crystallography data

The structure of Crystal Structure of the CDC25B Phosphatase Catalytic Domain with the Active Site Cysteine in the Sulfenic Form, PDB code: 1yml was solved by G.K.Buhrman, B.Parker, J.Sohn, J.Rudolph, C.Mattos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.78 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 49.867, 71.081, 74.300, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 20.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the CDC25B Phosphatase Catalytic Domain with the Active Site Cysteine in the Sulfenic Form (pdb code 1yml). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the CDC25B Phosphatase Catalytic Domain with the Active Site Cysteine in the Sulfenic Form, PDB code: 1yml:

Chlorine binding site 1 out of 1 in 1yml

Go back to Chlorine Binding Sites List in 1yml
Chlorine binding site 1 out of 1 in the Crystal Structure of the CDC25B Phosphatase Catalytic Domain with the Active Site Cysteine in the Sulfenic Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the CDC25B Phosphatase Catalytic Domain with the Active Site Cysteine in the Sulfenic Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1001

b:18.7
occ:1.00
 O A:HOH100 3.1 33.4 1.0
O A:HOH13 3.1 16.8 1.0
N A:GLU446 3.3 14.1 1.0
N A:ARG548 3.3 16.2 1.0
O A:HOH144 3.4 33.5 1.0
CA A:THR547 3.8 15.2 1.0
CB A:ARG548 3.8 23.4 1.0
CA A:LEU445 3.8 13.7 1.0
CD2 A:LEU445 3.9 15.7 1.0
CB A:GLU446 3.9 17.8 1.0
CB A:THR547 3.9 15.7 1.0
CG A:GLU446 3.9 22.5 1.0
C A:LEU445 4.0 12.7 1.0
C A:THR547 4.0 16.7 1.0
CA A:GLU446 4.2 15.0 1.0
CA A:ARG548 4.2 19.8 1.0
CB A:LEU445 4.3 14.2 1.0
NH1 A:ARG447 4.3 15.1 1.0
CG2 A:THR547 4.4 16.0 1.0
CD A:GLU446 4.6 24.7 1.0
O A:PRO444 4.7 15.1 1.0
CG A:LEU445 4.8 13.2 1.0
O A:HOH111 4.8 37.9 1.0
OE1 A:GLU446 5.0 27.0 1.0
N A:ARG447 5.0 14.7 1.0

Reference:

G.K.Buhrman, B.Parker, J.Sohn, J.Rudolph, C.Mattos. Structural Mechanism of Oxidative Regulation of the Phosphatase CDC25B Via An Intramolecular Disulfide Bond Biochemistry V. 44 5307 2005.
ISSN: ISSN 0006-2960
PubMed: 15807524
DOI: 10.1021/BI047449FS0006-2960(04)07449-5
Page generated: Thu Jul 10 20:45:29 2025

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